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CATH Superfamily 3.40.50.150

Vaccinia Virus protein VP39

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Vaccinia Virus protein VP39
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 135244: Sterol 24-C methyltransferase 2-2

There are 4 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Sterol 24-C-methyltransferase. [EC: 2.1.1.41]
S-adenosyl-L-methionine + 5-alpha-cholesta-8,24-dien-3-beta-ol = S-adenosyl-L-homocysteine + 24-methylene-5-alpha-cholest-8-en-3-beta-ol.
  • Acts on a range of sterols with a 24(25)-double bond in the side chain.
  • While zymosterol is the preferred substrate it also acts on desmosterol, 5-alpha-cholesta-7,24-dien-3-beta-ol, 5-alpha-cholesta- 5,7,24-trien-3-beta-ol, 4-alpha-methylzymosterol and others.
  • S-adenosyl-L-methionine attacks the Si face of the 24(25) double bond and the C-24 hydrogen is transferred to C-25 on the Re face of the double bond.
 622 A0A010RBE2 A0A010S5Y3 A0A014N590 A0A015JJN9 A0A017S0G8 A0A022VZX4 A0A022W865 A0A022XPY4 A0A022XYP3 A0A024SFN8
(612 more...)
24-methylenesterol C-methyltransferase. [EC: 2.1.1.143]
S-adenosyl-L-methionine + 24-methylenelophenol = S-adenosyl-L- homocysteine + (Z)-24-ethylidenelophenol.
  • This is the second methylation step of plant sterol biosynthesis (cf. EC 2.1.1.142).
 8 A0A0E0GGF5 A0A0E0NPD1 A0A178WGT2 A0A178WHI4 O82427 Q10S41 Q39227 Q94JS4
Squalene methyltransferase. [EC: 2.1.1.262]
2 S-adenosyl-L-methionine + squalene = 2 S-adenosyl-L-homocysteine + 3,22-dimethyl-1,2,23,24-tetradehydro-2,3,22,23-tetrahydrosqualene.
  • Two isoforms differing in their specificity were isolated from the green alga Botryococcus braunii BOT22.
  • TMT-1 gave more of the dimethylated form whereas TMT2 gave more of the monomethylated form.
 2 H2E7T5 H2E7T6
Botryococcene C-methyltransferase. [EC: 2.1.1.263]
2 S-adenosyl-L-methionine + C(30) botryococcene = 2 S-adenosyl-L- homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21- tetrahydrobotryococcene.
  • Isolated from the green alga Botryococcus braunii BOT22.
  • Shows a very weak activity with squalene.
 1 H2E7T7
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